Associations of allergenic soybean proteins with piglet skin allergic reaction and application of polyclonal antibodies
Chen Chi Chen A D , Tzu Tai Lee B D , Chin Bin Hsu C , Chien Wei Huang A and Bi Yu A E
+ Author Affiliations
- Author Affiliations
A Department of Animal Science, National Chung Hsing University, 250 Kuo Kuang Road, Taichung 402, Taiwan, R.O.C.
B Department of Biotechnology, Ming Dao University, Changhau 523, Taiwan, R.O.C.
C Kaohsiung Animal Propagation Station, Livestock Research Institute, Pingtung 912, Taiwan, R.O.C.
D These authors contributed equally to this work.
E Corresponding author. Email: byu@dragon.nchu.edu.tw
Animal Production Science 51(11) 1008-1014 https://doi.org/10.1071/AN11142
Submitted: 17 July 2011 Accepted: 30 August 2011 Published: 25 October 2011
Abstract
A skin prick test was conducted to evaluate the skin allergic reaction of piglets caused by allergenic proteins contained in soybean meal. The data accumulated from subcutaneous piglet skin tissue indicated that allergenic proteins contained in soybean meal crude extracts, even in low dosage levels (7 μg), caused immunological redness and inflammation within 5 min. The dosages above 200 μg of β-conglycinin caused inflammation covering a larger area. The glycinin had less of an influence on skin allergenic reaction dosages than β-conglycinin did. The antibodies used for β-conglycinin and glycinin subunits did not exhibit cross-recognition to other subunits or Leguminosae members, such as green beans, lupins and red beans. The polyclonal antibodies further indicated that some allergenic proteins were present after examining soybean meal fermented products individually by Aspergillus or Lactobacillus. None of the allergenic proteins were detected in soybean meal underwent two-stage fermentation. The skin prick test was found to be a convenient method for evaluating the skin allergic reaction of soy allergenic proteins in piglets. The produced polyclonal antibodies are based on subunits of allergenic proteins and can be used to detect the allergenic proteins present in soya products and soybean meal fermented products.
Additional keywords: fermentation, skin prick test, soybean meal.
References
Aguirre L, Garro MS, Savoy de Giori G (2008) Enzymatic hydrolysis of soybean protein using lactic acid bacteria. Food Chemistry 111, 976–982.| Enzymatic hydrolysis of soybean protein using lactic acid bacteria.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXosVaktbg%3D&md5=2e3b548206949e63008c4558ffb28621CAS |
Chen CC, Shih YC, Chiou PWS, Yu B (2010) Evaluating nutritional quality of single stage- and two stage-fermented soybean meal. Asian-Australasian Journal of Animal Sciences 23, 598–606.
Dreau D, Lalles JP, Philouze-Rome V, Toullec R, Salmon H (1994) Local and systemic immune responses to soybean protein ingestion in early-weaned pigs. Journal of Animal Science 72, 2090–2098.
Frias J, Song YS, Martínez-Villaluenga C, González de Mejia E, Vidal-Valverde C (2008) Immunoreactivity and amino acid content of fermented soybean products. Journal of Agricultural and Food Chemistry 56, 99–105.
| Immunoreactivity and amino acid content of fermented soybean products.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXhsVWqsb7J&md5=a31616ad49ac8812622bd8969e023bc0CAS |
Friedman M, Brandon DL (2001) Nutritional and health benefits of soy proteins. Journal of Agricultural and Food Chemistry 49, 1069–1086.
Fu CJ, Jez JM, Kerley MS, Allee GL, Krishnan HB (2007) Identification, characterization, epitope mapping, and three-dimensional modeling of the alpha-subunit of beta-conglycinin of soybean, a potential allergen for young pigs. Journal of Agricultural and Food Chemistry 55, 4014–4020.
| Identification, characterization, epitope mapping, and three-dimensional modeling of the alpha-subunit of beta-conglycinin of soybean, a potential allergen for young pigs.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXkt1elsLs%3D&md5=bc52416b6b50eab741a448b3784143caCAS |
Helm RM, Furuta GT, Stanley JS, Ye J, Cockrell G, Connaughton C, Simpson P, Bannon GA, Burks AW (2002) A neonatal swine model for peanut allergy. The Journal of Allergy and Clinical Immunology 109, 136–142.
| A neonatal swine model for peanut allergy.Crossref | GoogleScholarGoogle Scholar |
Hrckova M, Rusoakova M, Zemanovi J (2002) Enzymatic hydrolysis of defatted soy flour by three different proteases and their effect on the functional properties of resulting protein hydrolysates. Czech Journal of Food Sciences 20, 7–14.
Joa PS, Freire JB, Ferreira RB, Seabra M, Teixeira A, Toullec R, Lalles JP (2002) Legume proteins of the vicilin family are more immunogenic than those of the legumin family in weaned piglets. Food and Agricultural Immunology 14, 51–63.
| Legume proteins of the vicilin family are more immunogenic than those of the legumin family in weaned piglets.Crossref | GoogleScholarGoogle Scholar |
Jones CK, Derouchey JM, Nelssen JL, Tokach MD, Dritz SS, Goodband RD (2010) Effects of fermented soybean meal and specialty animal protein sources on nursery pig performance. Journal of Animal Science 88, 1725–1732.
| Effects of fermented soybean meal and specialty animal protein sources on nursery pig performance.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXlsVWku7c%3D&md5=b99ef71245a36c4a54863bf88a231c19CAS |
Krishnan HB, Kim WS, Jang S, Kerley MS (2009) All three subunits of soybean beta-conglycinin are potential food allergens. Journal of Agricultural and Food Chemistry 57, 938–943.
| All three subunits of soybean beta-conglycinin are potential food allergens.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1MXksVyktA%3D%3D&md5=070e48eaaac82c7f95ad51a1f2b40cf3CAS |
Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685.
| Cleavage of structural proteins during the assembly of the head of bacteriophage T4.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXlsFags7s%3D&md5=b9dba7a188ce8d9cb8ff534fce0d2fb0CAS |
Lee HW, Keum EH, Lee SJ, Sung DE, Chung DH, Lee SI, Oh S (2007a) Allergenicity of proteolytic hydrolysates of the soybean 11S globulin. Journal of Food Science 72, C168–C172.
| Allergenicity of proteolytic hydrolysates of the soybean 11S globulin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD2sXkslGhs7w%3D&md5=4cf2f38441037de06425d9d0e573be72CAS |
Lee TTT, Morisset M, Moneret-Vautrin D-A, Astier C, Cordebar V, Codreanu F, Beaudouin E, Bihain BE, Kanny G (2007b) Contamination of probiotic preparations with milk allergen can cause anaphylaxis in cow’s milk allergic patients. The Journal of Allergy and Clinical Immunology 119, 746–747.
| Contamination of probiotic preparations with milk allergen can cause anaphylaxis in cow’s milk allergic patients.Crossref | GoogleScholarGoogle Scholar |
Lee TT, Chang CC, Juang RS, Chen RB, Yang SY, Chu LW, Wang SR, Wang CS, Tseng TH, Chen LJ, Yu B (2010) Porcine lactoferrin expression in transgenic rice and its effects as a feed additive on early weaned piglets. Journal of Agricultural and Food Chemistry 58, 5166–5173.
| Porcine lactoferrin expression in transgenic rice and its effects as a feed additive on early weaned piglets.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXjvVeisrk%3D&md5=633e9bfd27aad66a2bae42e4dc9f9d84CAS |
Li DF, Nelssen JL, Reddy PG, Blecha F, Klemm RD, Giesting DW, Hancock JD, Allee GL, Goodband RD (1991) Measuring suitability of soybean products for early-weaned pigs with immunological criteria. Journal of Animal Science 69, 3299–3307.
Lowry QH, Rosebrough NJ, Farr LA, Randall RJ (1951) Protein measurement with the folin phenol reagent. The Journal of Biological Chemistry 193, 256–275.
Maruyama N, Mohamed Salleh MR, Takahashi K, Yagasaki K, Goto H, Hontani N, Nakagawa S, Utsumi S (2002) Structure physicochemical function relationships of soybean β-conglycinin heterotrimers. Journal of Agricultural and Food Chemistry 50, 4323–4326.
| Structure physicochemical function relationships of soybean β-conglycinin heterotrimers.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38Xks1aru78%3D&md5=965a497f3ff3d18e7c95d64f5c23868dCAS |
Maruyama N, Okuda E, Tatsuhara M, Utsumi S (2008) Aggregation of proteins having Golgi apparatus sorting determinant induced large globular structures derived from the endoplasmic reticulum in plant seed cells. FEBS Letters 582, 1599–1606.
| Aggregation of proteins having Golgi apparatus sorting determinant induced large globular structures derived from the endoplasmic reticulum in plant seed cells.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXlslyis70%3D&md5=4919bbc7ec5dfb73d9081c141ea393b8CAS |
Matoba N, Doyama N, Yamada Y, Maruyama N, Utssumi S, Yoshikawa M (2001) Design and production of genetically modified soybean protein with anti-hypertensive activity by incorporating potent analogue of ovokinin. FEBS Letters 497, 50–54.
| Design and production of genetically modified soybean protein with anti-hypertensive activity by incorporating potent analogue of ovokinin.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXjslent7s%3D&md5=59832811573cb5d8c1b5f588d9461a42CAS |
Mendoza EM, Adachi TM, Bernardo AEN, Utsumi S (2001) Mungbean [Vigna radiata (L.) Wilczek] globulins: purification and characterization. Journal of Agricultural and Food Chemistry 49, 1552–1558.
| Mungbean [Vigna radiata (L.) Wilczek] globulins: purification and characterization.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD3MXhtl2ktL4%3D&md5=5c733b62617e84994a42a895b6a776c8CAS |
Meng G, Ma CY (2002) Characterization of globulin from Phaseolus angularis (red bean). International Journal of Food Science & Technology 37, 687–695.
| Characterization of globulin from Phaseolus angularis (red bean).Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XntFOrurw%3D&md5=16021a224e9787ea1a4098b716c4d070CAS |
Motoyama T, Maruyama N, Amari Y, Kobayashi K, Washida H, Higasa T, Takaiwa F, Utsumi S (2009) α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds. Journal of Experimental Botany 60, 4015–4027.
| α′ Subunit of soybean β-conglycinin forms complex with rice glutelin via a disulphide bond in transgenic rice seeds.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1MXht1WqtLbF&md5=ef7ed141eaac5acba0f40d906faa950eCAS |
Nagano T, Hirotsuka M, Mori H, Kohyama K, Nishinarit K (1992) Dynamic viscoelastic study on the gelation of 7S globulin from soybeans. Journal of Agricultural and Food Chemistry 40, 941–944.
| Dynamic viscoelastic study on the gelation of 7S globulin from soybeans.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DyaK38XktVKgsbs%3D&md5=56a5e95cb10b17616467c50a93d2e45aCAS |
Ogawa A, Samoto M, Takahashi K (2000) Soybean allergens and hypoallergenic soybean products. Journal of Nutritional Science and Vitaminology 46, 271–279.
Onilude AA, Sanni AI, Ighalo MI (1999) Effect of process improvement on the physico-chemical properties of infant weaning food from fermented composite blends of cereal and soybeans. Plant Foods for Human Nutrition (Dordrecht, Netherlands) 54, 239–250.
| Effect of process improvement on the physico-chemical properties of infant weaning food from fermented composite blends of cereal and soybeans.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DC%2BD3c7nvFWnuw%3D%3D&md5=adf4516f3c0ce2e2205ab3bdc1ca0087CAS |
SAS (1999) ‘User’s guide. Version 8.’ (SAS Institute Inc.: Cary, NC)
Song YS, Frias J, Martinez-Villaluenga C, Vidal-Valdeverde C, Gonzalez de Mejia E (2008) Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products. Food Chemistry 108, 571–581.
| Immunoreactivity reduction of soybean meal by fermentation, effect on amino acid composition and antigenicity of commercial soy products.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXnvVKjsQ%3D%3D&md5=b4bfa5e4b262270ccffd523b8edd66a7CAS |
Song YS, Pérez VG, Pettigrew JE, Martinez-Villaluenga C, Gonzalez de Mejia E (2010) Fermentation of soybean meal and its inclusion in diets for newly weaned pigs reduced diarrhea and measures of immunoreactivity in the plasma. Animal Feed Science and Technology 159, 41–49.
| Fermentation of soybean meal and its inclusion in diets for newly weaned pigs reduced diarrhea and measures of immunoreactivity in the plasma.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BC3cXosVGntrg%3D&md5=5802c364195b6b19a0f80aeb9c6a995aCAS |
Songré-Ouattara LT, Mouquet-Rivier C, Icard-Vernière C, Humblot C, Diawara B, Guyot JP (2008) Enzyme activities of lactic acid bacteria from a pearl millet fermented gruel (ben-saalga) of functional interest in nutrition. International Journal of Food Microbiology 128, 395–400.
| Enzyme activities of lactic acid bacteria from a pearl millet fermented gruel (ben-saalga) of functional interest in nutrition.Crossref | GoogleScholarGoogle Scholar |
Thanh VH, Shibasaki K (1976) Major proteins of soybean seeds. A straightforward fractionation and their characterization. Journal of Agricultural and Food Chemistry 24, 1117–1121.
| Major proteins of soybean seeds. A straightforward fractionation and their characterization.Crossref | GoogleScholarGoogle Scholar | 1:STN:280:DyaE2s%2FntF2mtQ%3D%3D&md5=d3356362c2ba388bcef20132d530b416CAS |
Zhang GY, Hayashi Y, Matsumoto S, Matsumura Y, Mori T (2002) Molecular species of glycinin in some soybean cultivars. Phytochemistry 60, 675–681.
| Molecular species of glycinin in some soybean cultivars.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD38XlsVKhsrY%3D&md5=c60904a3dbf25255affde0b937f5daffCAS |
Zhao Y, Qin G, Sun Z, Zhang X, Bao N, Wang T, Zhang B, Zhang B, Zhu D, Sun L (2008) Disappearance of immunoreactive glycinin and beta-conglycinin in the digestive tract of piglets. Archives of Animal Nutrition 62, 322–330.
| Disappearance of immunoreactive glycinin and beta-conglycinin in the digestive tract of piglets.Crossref | GoogleScholarGoogle Scholar | 1:CAS:528:DC%2BD1cXosFagsrk%3D&md5=bec5513cc0ba4fc677295c5103b8c96dCAS |
Žilić SM, Barać MB, Pesić MB, Mladenović Drinić SD, Ignjatović-Micić DD, Srebrić MB (2011) Characterization of proteins from kernel of different soybean varieties. Journal of the Science of Food and Agriculture 91, 60–67.
| Characterization of proteins from kernel of different soybean varieties.Crossref | GoogleScholarGoogle Scholar |
